Enzyme-catalyzed synthesis of a bioactive oligopeptide in nearly anhydrous solvents with polyethylene glycol-modified proteases.
An oligopeptide, L-arginyl-glycyl-L-aspartyl-L-serine, having cell attachment activity was synthesized from the respective aminoacids carrying suitable protecting residues, by using carboxymethyl polyethylene glycol (PEG)-modified proteases in organic solvents. Papain, trypsin, and alpha-chymotrypsin were modified with PEG. Organic solvents used were 1,1,1-trichloroethane, chloroform and chloroform/ethyl cellosolve (1:1) mixture. Identification of the products was done by gel permeation chromatography (GPC) and thin layer chromatography (TLC).
Nakajima
A
A
Department of Applied Chemistry, Osaka Institute of Technology, Japan.
Hirano
Y
Y
Terai
T
T
Goto
K
K
Hayashi
T
T
Ikada
Y
Y
D000595:Amino Acid Sequence; D001672:Biocompatible Materials; D002918:Chymotrypsin / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D007202:Indicators and Reagents; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis*; D010206:Papain / Q000378:metabolism; D011092:Polyethylene Glycols / Q000494:pharmacology*; D012997:Solvents; D014357:Trypsin / Q000378:metabolism
D001672:Biocompatible Materials; D007202:Indicators and Reagents; D009842:Oligopeptides; D012997:Solvents; D011092:Polyethylene Glycols; D010450:Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin; D010206:Papain